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Literature summary for 6.3.4.10 extracted from

  • Healy, S.; Heightman, T.D.; Hohmann, L.; Schriemer, D.; Gravel, R.A.
    Nonenzymatic biotinylation of histone H2A (2009), Protein Sci., 18, 314-328.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 6.3.4.10

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm
-
 Homo sapiens 5737
-
nucleus
-
 Homo sapiens 5634
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
 Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + biotin + apo-[propionyl-CoA carboxylase] substrate is p67, the carboxyl-terminal fragment of the propionyl-CoA-carboxylase alpha subunit, the substrate is biotinylated at Lys67 Homo sapiens AMP + diphosphate + propionyl-CoA carboxylase
-
 ?
ATP + biotin + BCCP87 substrate is the biotinoyl domain, BCCP87, of Escherichia coli biotin carboxyl carrier protein, BCCP, binding pattern, overview Homo sapiens AMP + diphosphate + biotin-BCCP87
-
 ?
ATP + biotin + histone H2A pattern of biotin attachment and comparison to nonenzymatic biotinylation of histone H2A, none of the lysine sites within histone H2A resembles the biotin attachment consensus sequence seen in carboxylases, mechanism, overview. H2A is a poor substrate for biotin attachment compared to the apocarboxylase biotin-attachment domain Homo sapiens AMP + diphosphate + biotin-histone H2A
-
 ?

Synonyms

Synonyms Comment Organism
biotin protein ligase
-
 Homo sapiens
HCS
-
 Homo sapiens
Holocarboxylase synthetase
-
 Homo sapiens

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Homo sapiens